PD-L1 Reverse Signaling in Dermal Dendritic Cells Promotes Dendritic Cell Migration Required for Skin Immunity.
Actins
/ metabolism
Amino Acids
/ genetics
Animals
B7-H1 Antigen
/ chemistry
Base Sequence
CD8-Positive T-Lymphocytes
/ immunology
Cell Count
Cell Movement
/ drug effects
Chemokine CCL21
/ pharmacology
Chemotaxis
/ drug effects
Dendritic Cells
/ drug effects
Dermis
/ cytology
Exons
/ genetics
Extracellular Signal-Regulated MAP Kinases
/ metabolism
GTP-Binding Proteins
/ metabolism
Immunity
/ drug effects
Lymph Nodes
/ metabolism
Mice, Inbred C57BL
Mutation
/ genetics
Phosphorylation
/ drug effects
Poly I-C
/ pharmacology
Polymerization
Protein Domains
Receptors, CCR7
/ metabolism
Signal Transduction
/ drug effects
CCR7 signaling
G alpha activation
MAPK signaling
PD-L1 reverse signaling
actin polymerization
dendritic cell migration
dendritic cell trafficking
dermal dendritic cell
infection
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
13 10 2020
13 10 2020
Historique:
received:
07
05
2020
revised:
06
08
2020
accepted:
21
09
2020
entrez:
14
10
2020
pubmed:
15
10
2020
medline:
22
9
2021
Statut:
ppublish
Résumé
Although the function of the extracellular region of programmed death ligand 1 (PD-L1) through its interactions with PD-1 on T cells is well studied, little is understood regarding the intracellular domain of PD-L1. Here, we outline a major role for PD-L1 intracellular signaling in the control of dendritic cell (DC) migration from the skin to the draining lymph node (dLN). Using a mutant mouse model, we identify a TSS signaling motif within the intracellular domain of PD-L1. The TSS motif proves critical for chemokine-mediated DC migration to the dLN during inflammation. This loss of DC migration, in the PD-L1 TSS mutant, leads to a significant decline in T cell priming when DC trafficking is required for antigen delivery to the dLN. Finally, the TSS motif is required for chemokine receptor signaling downstream of the Gα subunit of the heterotrimeric G protein complex, ERK phosphorylation, and actin polymerization in DCs.
Identifiants
pubmed: 33053342
pii: S2211-1247(20)31247-X
doi: 10.1016/j.celrep.2020.108258
pmc: PMC7688291
mid: NIHMS1638448
pii:
doi:
Substances chimiques
Actins
0
Amino Acids
0
B7-H1 Antigen
0
Ccr7 protein, mouse
0
Chemokine CCL21
0
Receptors, CCR7
0
Extracellular Signal-Regulated MAP Kinases
EC 2.7.11.24
GTP-Binding Proteins
EC 3.6.1.-
Poly I-C
O84C90HH2L
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108258Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK125595
Pays : United States
Organisme : NIAID NIH HHS
ID : T32 AI007405
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM136444
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008730
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI155474
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI121209
Pays : United States
Informations de copyright
Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.
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